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Interplay Between PEO Tether Length and Ligand Spacing Governs Cell Spreading on RGD-Modified PMMA-g-PEO Comb Copolymers

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Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, and Department of Mechanical Engineering and Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139
Cite this: Biomacromolecules 2007, 8, 10, 3206–3213
Publication Date (Web):September 18, 2007
https://doi.org/10.1021/bm070237o
Copyright © 2007 American Chemical Society
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Abstract

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The effects of tether length on cell adhesion to poly(methyl methacrylate)-graft-poly(ethylene oxide), PMMA-g-PEO, comb copolymer films functionalized with the adhesion peptide RGD were investigated. Copolymers having PEO tether lengths of 10 and 22 EO segments were synthesized and coupled with a synthetic peptide that contained both RGD and the synergy sequence PHSRN. Cell spreading assays revealed that the longer polymer tethers increased the rate of spreading and reduced the time required for fibroblasts to form focal adhesions. Fluorescence resonance energy transfer (FRET) measurements indicated a mean separation between integrin-bound peptides of 15.6 ± 1.4 nm for combs with long (22-mer) tethers, compared with 17.5 ± 1.3 nm for short (10-mer) tethers, on films of comparable peptide density (∼2500 peptides/μm2). The results suggest that the added mobility afforded by the more extensible tethers encouraged the formation of focal adhesions by allowing cells to reorganize tethered peptides on the nanometer length scale. In addition, adhesion peptides were selectively coupled to 10-mer or 22-mer PEO tethers within a bimodal brush to investigate stratification effects on cell adhesion. Peptides bound by short tethers in a bed of long unsubstituted chains resulted in surfaces that resisted, rather than promoted, cell adhesion. By contrast, when long peptide tethers were employed with short unsubstituted chains, cell attachment and spreading were comparable to that found on a monomodal brush of long chains at equivalent peptide density.

†

 Department of Materials Science and Engineering.

‡

 Department of Mechanical Engineering and Department of Biological Engineering.

*

 Corresponding author. E-mail:  [email protected]

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